SAS-6 is a cartwheel protein that establishes the 9-fold symmetry of the centriole
SAS-6 is a cartwheel protein that establishes the 9-fold symmetry of the centriole
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DOI:
10.1016/j.cub.2007.11.046
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发表时间:
2007-12-18
期刊:
影响因子:
9.2
通讯作者:
Hirono, Masafumi
中科院分区:
文献类型:
--
作者:
Nakazawa, Yuki;Hiraki, Madoka;Hirono, Masafumi
Centrioles consist of nine-triplet microtubules arranged in rotational symmetry. This structure is highly conserved among various eukaryotic organisms and serves as the base for the ciliary axoneme. Recently, several proteins such as SAS-6 have been identified as essential to the early process of centriole assembly [1, 2], but the mechanism that produces the 9-fold symmetry is poorly understood. In C. elegans and Drosophila, SAS-6 has been suggested to function in the formation of a centriolar precursor, a central tube that then assembles nine-singlet microtubules on its surface. However, the generality of the central tube is not clear because in many other organisms, the first structure appearing in the centriole assembly is not a tube but a flat amorphous ring or a cartwheel-structure with a hub and nine radiating spokes. Here we show that in Chlamydomonas the SAS-6 protein localizes to the central part of the cartwheel and that a null mutant of SAS-6, bld12, lacks that part. Intriguingly, this mutant frequently has centrioles; composed of 7,8, 10, or 11 triplets in addition to 9-triplet centrioles. We presume that, in many organisms, SAS-6 is an essential component of the cartwheel, a structure that stabilizes the 9-triplet structure.